Maggot chymotrypsin I from Lucilia sericata is resistant to endogenous wound protease inhibitors.
Br J Dermatol
; 164(1): 192-6, 2011 Jan.
Article
em En
| MEDLINE
| ID: mdl-21175562
ABSTRACT
BACKGROUND:
A chymotrypsin found in the secretions of Lucilia sericata and manufactured as a recombinant enzyme degrades chronic wound eschar ex vivo.OBJECTIVES:
To characterize the inhibition profile of the L. sericata recombinant chymotrypsin I.METHODS:
Activity of recombinant chymotrypsin I and its sensitivity to endogenous inhibitors were determined enzymatically using the fluorogenic substrate succinyl-alanyl-alanyl-prolyl-phenylalanyl-aminomethyl coumarin.RESULTS:
We report the presence of high concentrations of two endogenous inhibitors, α1-antichymotrypsin and α1-antitrypsin, in wound eschar and a trace of a third, α2-macroglobulin, with the potential to inhibit this debridement process. However, the addition of a soluble and inhibitor-containing extract of chronic wound eschar to chymotrypsin I did not affect activity of the enzyme, neither did the addition of purified native α1-antichymotrypsin or α1-antitrypsin, although chymotrypsin I was inhibited by α2-macroglobulin. Conversely, the mammalian equivalent, α-chymotrypsin, was inhibited by the purified native α1-antichymotrypsin, α1-antitrypsin and α2-macroglobulin and by the soluble extract of wound eschar.CONCLUSIONS:
The data suggest that the maggot-derived chymotrypsin I is biochemically distinct from human α-chymotrypsin and the lack of inhibition by wound eschar suggests a means by which chymotrypsin I activity survives within the wound to contribute towards debridement during maggot biotherapy.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pele
/
Ferimentos e Lesões
/
Quimotripsina
/
Inibidores da Tripsina
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Dípteros
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Br J Dermatol
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Reino Unido